Abstract
P2X receptors are ion channels gated by extracellular ATP. We report here cloning of a P2X(2) receptor splice variant (P2X(2-2)) carrying a 207 bp deletion in the intracellular C-terminus and the analysis of the corresponding genomic structure of the P2X(2) gene. P2X(2-2) is as highly expressed as the original P2X(2) sequence in various tissues. ATP-activated currents mediated by heterologous expressed P2X(2) or P2X(2-2) receptors showed significant differences in desensitization time constants and steady-state currents in the continuous presence of ATP. These results imply functional differences between cells differentially expressing these P2X(2) isoforms.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Adenosine Triphosphate / pharmacology
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Alternative Splicing*
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Amino Acid Sequence
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Animals
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Base Sequence
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Brain / metabolism
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Cell Line
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Female
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Genetic Variation
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Humans
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Intestinal Mucosa / metabolism
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Kidney / metabolism
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Membrane Potentials / drug effects
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Molecular Sequence Data
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Mutagenesis, Site-Directed
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Oocytes / physiology
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Organ Specificity
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Organ of Corti / metabolism
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Patch-Clamp Techniques
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Rats
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Rats, Wistar
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Receptors, Purinergic P2 / biosynthesis
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Receptors, Purinergic P2 / chemistry
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Receptors, Purinergic P2 / physiology*
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Receptors, Purinergic P2X2
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Recombinant Proteins / biosynthesis
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Recombinant Proteins / chemistry
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Recombinant Proteins / metabolism
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Sequence Deletion
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Spleen / metabolism
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Transfection
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Xenopus laevis
Substances
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P2RX2 protein, human
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Receptors, Purinergic P2
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Receptors, Purinergic P2X2
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Recombinant Proteins
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Adenosine Triphosphate